Alexandre, Kabamba B.Gray, Elin Solomonovna.Lambson, Bronwen Elizabeth.Moore, Penelope L.Choge, Isaac Ang'Ang'A.Mlisana, Koleka Patience.Abdool Karim, Salim Safurdeen.McMahon, James.O'Keefe, Barry.Chikwamba, Rachel.Morris, Lynn.2012-11-292012-11-2920102010Alexandre, K.B. et al. 2010. Mannose-rich glycosylation patterns on HIV-1 subtype C gp120 and sensitivity to the lectins, Griffithsin, Cyanovirin-N and Scytovirin. Virology 402 (1), pp. 187–196.0042-6822http://dx.doi.org/10.1016/j.virol.2010.03.021http://hdl.handle.net/10413/8042Griffithsin (GRFT), Cyanovirin-N (CV-N) and Scytovirin (SVN) are lectins that inhibit HIV-1 infection by binding to multiple mannose-rich glycans on the HIV-1 envelope glycoproteins (Env). Here we show that these lectins neutralize subtype C primary virus isolates in addition to Env-pseudotyped viruses obtained from plasma and cervical vaginal lavages. Among 15 subtype C pseudoviruses, the median IC50 values were 0.4, 1.8 and 20.1 nM for GRFT, CV-N and SVN, respectively, similar to what was found for subtype B and A. Analysis of Env sequences suggested that concomitant lack of glycans at positions 234 and 295 resulted in natural resistance to these compounds, which was confirmed by site-directed mutagenesis. Furthermore, the binding sites for these lectins overlapped that of the 2G12 monoclonal antibody epitope, which is generally absent on subtype C Env. This data support further research on these lectins as potential microbicides in the context of HIV-1 subtype C infection.enHIV (Viruses)Griffithsin.Cyanovirin-N.Scytovirin.HIV-1 subtype C.Microbicides.2G12 monoclonal antibody.Peer reviewed journal article